Characterization of Bacillus thuringiensis Cry toxin binding novel GPI anchored aminopeptidase from fat body of the moth Spodoptera litura

Madhusudhan Budatha, Gargi Meur, P. B. Kirti, Aparna Dutta Gupta

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

Aminopeptidase N (APN) isoforms were identified as candidate receptors for Bacillus thuringiensis Cry toxins from the midgut of several insect species. In this study a partial cDNA encoding aminopeptidase (slfbAPN) was cloned from fat body of the moth Spodoptera litura. In the deduced amino acid sequence the characteristic metallopeptidase sequences, HEXXHX18E and GAMENWG were conserved but the sequence showed only 33-39% identity to other insect APNs, which were also reported to be Cry toxin receptors. The presence of a putative GPI anchor signal sequence at the C-terminus indicated that it is a membrane-anchored protein. The slfbAPN expression was restricted to the fat body as suggested by northern blot analysis of different tissues. Biochemical analyses including immunoblotting, ligand blotting and lectin blotting, demonstrated that slfbAPN is a membrane-anchored glycoprotein in the fat body and it binds to Cry toxins.

Original languageEnglish (US)
Pages (from-to)1651-1657
Number of pages7
JournalBiotechnology Letters
Volume29
Issue number11
DOIs
StatePublished - Nov 1 2007
Externally publishedYes

Keywords

  • Aminopeptidase
  • Bacillus thuringiensis
  • Cry toxin
  • Fat body
  • GPI anchor
  • Spodoptera litura

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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